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Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach

The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protei...

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Detalles Bibliográficos
Autores principales: Singh, Ashutosh, Orsat, Valérie, Raghavan, Vijaya
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030879/
https://www.ncbi.nlm.nih.gov/pubmed/24970163
http://dx.doi.org/10.3390/biom3010168
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author Singh, Ashutosh
Orsat, Valérie
Raghavan, Vijaya
author_facet Singh, Ashutosh
Orsat, Valérie
Raghavan, Vijaya
author_sort Singh, Ashutosh
collection PubMed
description The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protein isolate but the higher electric field strength of 3 V/nm significantly affected the protein conformation and solvent accessible surface area. The response of protein isolate to various external field stresses demonstrated that it is necessary to gain insight into protein dynamics under electromagnetic fields in order to be able to develop the techniques utilizing them for food processing and other biological applications.
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spelling pubmed-40308792014-06-24 Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach Singh, Ashutosh Orsat, Valérie Raghavan, Vijaya Biomolecules Article The molecular dynamic (MD) modeling approach was applied to evaluate the effect of an external electric field on soybean hydrophobic protein and surface properties. Nominal electric field strengths of 0.002 V/nm and 0.004 V/nm had no major effect on the structure and surface properties of the protein isolate but the higher electric field strength of 3 V/nm significantly affected the protein conformation and solvent accessible surface area. The response of protein isolate to various external field stresses demonstrated that it is necessary to gain insight into protein dynamics under electromagnetic fields in order to be able to develop the techniques utilizing them for food processing and other biological applications. MDPI 2013-02-11 /pmc/articles/PMC4030879/ /pubmed/24970163 http://dx.doi.org/10.3390/biom3010168 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Singh, Ashutosh
Orsat, Valérie
Raghavan, Vijaya
Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title_full Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title_fullStr Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title_full_unstemmed Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title_short Soybean Hydrophobic Protein Response to External Electric Field: A Molecular Modeling Approach
title_sort soybean hydrophobic protein response to external electric field: a molecular modeling approach
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4030879/
https://www.ncbi.nlm.nih.gov/pubmed/24970163
http://dx.doi.org/10.3390/biom3010168
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